Inhibition of arylsulfatase B by ascorbic acid.

One hypothesis for atherosclerotic lesion formation is the response to injury hypothesis. If catabolism of the ground substance of the intima of blood vessels is viewed as an injury, then inhibition of this catabolism could lead to a decrease in atherosclerotic lesions. Arylsulfatase B catalyses the desulfation of glycosaminoglycans in the catabolism of the intimal ground substance.

Spectral displacement techniques for studying the binding of spectroscopically transparent ligands to cyclodextrins.

A spectroscopic displacement method is used to determine association constants of beta-cyclodextrin with compounds that are spectroscopically transparent. These compounds are adamantanecarboxylate and structurally related compounds. Association constants obtained are compared to values obtained by other methods.

Fluorescence quenching of liver alcohol dehydrogenase by acrylamide.

The quenching of the fluorescence of liver alcohol dehydrogenase by acrylamide has been studied as a function of excitation and emission wavelength. Downward curving Stern-Volmer plots are found, providing further support for the notion that Trp-15 of the protein is surface exposed and that Trp-314 is extensively buried within the protein. The acrylamide quenching of the binary complex formed between the protein and NAD+ was also studied.

Mechanism of adsorption and eclipse of bacteriophage phi X174. II. Attachment and eclipse with isolated Escherichia coli cell wall lipopolysaccharide.

A mixture of aqueous phenol, choloroform, and ether extracts the lipopolysaccharides (LPS) from the phiX174-sensitive strain, Escherichia coli C/1, and resistant strains, C/phiX and K12. Interaction of the C/1 LPS with phiX in a starvation buffer containing 10(-3) M CaCl(2) at 37 C, but not at 15 C, results in a first-order inactivation that is specific for C/1 LPS. After interaction for 60 min at 15 C, followed by centrifugation, 37 and 20% of a (14)C-phiX preparation are bound to the C/1 and C/phiX LPS pellets, respectively.